Q9BWP8 · COL11_HUMAN
- ProteinCollectin-11
- GeneCOLEC11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids271 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lectin that plays a role in innate immunity, apoptosis and embryogenesis (PubMed:21258343, PubMed:23954398, PubMed:25912189).
Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope (PubMed:25912189).
Primarily recognizes the terminal disaccharide of the glycan (PubMed:25912189).
Also recognizes a subset of fucosylated glycans and lipopolysaccharides (PubMed:17179669, PubMed:25912189).
Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1 (PubMed:20956340, PubMed:25912189).
Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding (Probable). Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis (PubMed:21258343, PubMed:28301481).
Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope (PubMed:25912189).
Primarily recognizes the terminal disaccharide of the glycan (PubMed:25912189).
Also recognizes a subset of fucosylated glycans and lipopolysaccharides (PubMed:17179669, PubMed:25912189).
Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1 (PubMed:20956340, PubMed:25912189).
Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding (Probable). Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis (PubMed:21258343, PubMed:28301481).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 200 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 207 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 211 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 211 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 232 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 234 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 235 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 238 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 240 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 240 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 240 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 241 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 241 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 252 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 252-254 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: NDV | ||||||
Binding site | 253 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | collagen trimer | |
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | serine-type endopeptidase complex | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent carbohydrate binding | |
Molecular Function | D-mannose binding | |
Molecular Function | DNA binding | |
Molecular Function | fucose binding | |
Molecular Function | identical protein binding | |
Molecular Function | oligosaccharide binding | |
Biological Process | antimicrobial humoral response | |
Biological Process | cell surface pattern recognition receptor signaling pathway | |
Biological Process | complement activation | |
Biological Process | complement activation, lectin pathway | |
Biological Process | developmental process | |
Biological Process | execution phase of apoptosis | |
Biological Process | positive regulation of opsonization | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCollectin-11
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BWP8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
3MC syndrome 2 (3MC2)
- Note
- DescriptionA form of 3MC syndrome, an autosomal recessive disorder characterized by facial dysmorphism, craniosynostosis, learning disability, and genital, limb and vesicorenal anomalies. Facial features include hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes.
- See alsoMIM:265050
Natural variants in 3MC2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078813 | 166 | A>T | in 3MC2; uncertain significance | |
VAR_065901 | 169 | S>P | in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis; dbSNP:rs387907075 | |
VAR_065902 | 204 | G>S | in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis; dbSNP:rs387907076 | |
VAR_065903 | 217 | missing | in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_078813 | 166 | in 3MC2; uncertain significance | |||
Sequence: A → T | ||||||
Natural variant | VAR_065901 | 169 | in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis; dbSNP:rs387907075 | |||
Sequence: S → P | ||||||
Natural variant | VAR_065902 | 204 | in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis; dbSNP:rs387907076 | |||
Sequence: G → S | ||||||
Natural variant | VAR_065903 | 217 | in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis | |||
Sequence: Missing | ||||||
Natural variant | VAR_038143 | 219 | in dbSNP:rs7567833 | |||
Sequence: H → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 391 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MRGNLALVGVLISLAFLSLLPSGHP | ||||||
Chain | PRO_0000315044 | 26-271 | Collectin-11 | |||
Sequence: QPAGDDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEKGDMGDKGQKGSVGRHGKIGPIGSKGEKGDSGDIGPPGPNGEPGLPCECSQLRKAIGEMDNQVSQLTSELKFIKNAVAGVRETESKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRTFNKWRSGEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMCEFDKENM | ||||||
Disulfide bond | 170↔264 | |||||
Sequence: CQGRGGTLSMPKDEAANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRTFNKWRSGEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMC | ||||||
Disulfide bond | 242↔256 | |||||
Sequence: CVEMVASGGWNDVAC |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homotrimer; disulfide-linked (PubMed:20956340, PubMed:25912189).
Interacts with MASP1; probably triggers the lectin pathway of complement (PubMed:20956340).
Interacts with MASP1; probably triggers the lectin pathway of complement (PubMed:20956340).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BWP8 | COLEC10 Q9Y6Z7 | 3 | EBI-25809731, EBI-21859492 | |
BINARY | Q9BWP8 | COLEC11 Q9BWP8 | 5 | EBI-25809731, EBI-25809731 | |
BINARY | Q9BWP8 | MASP1 P48740 | 2 | EBI-25809731, EBI-6380536 | |
BINARY | Q9BWP8 | MASP1 P48740-1 | 2 | EBI-25809731, EBI-16138717 | |
BINARY | Q9BWP8 | MASP1 P48740-2 | 3 | EBI-25809731, EBI-26435098 | |
BINARY | Q9BWP8 | MASP2 O00187 | 3 | EBI-25809731, EBI-7965040 | |
BINARY | Q9BWP8-1 | C1QTNF6 Q9BXI9-2 | 3 | EBI-27104870, EBI-27104631 | |
BINARY | PRO_0000315044 | UMOD P07911 | 2 | EBI-26568155, EBI-2819647 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 44-113 | Disordered | ||||
Sequence: GDAGEKGDKGAPGRPGRVGPTGEKGDMGDKGQKGSVGRHGKIGPIGSKGEKGDSGDIGPPGPNGEPGLPC | ||||||
Domain | 65-112 | Collagen-like | ||||
Sequence: GEKGDMGDKGQKGSVGRHGKIGPIGSKGEKGDSGDIGPPGPNGEPGLP | ||||||
Coiled coil | 114-148 | |||||
Sequence: ECSQLRKAIGEMDNQVSQLTSELKFIKNAVAGVRE | ||||||
Domain | 149-265 | C-type lectin | ||||
Sequence: TESKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRTFNKWRSGEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMCE |
Sequence similarities
Belongs to the COLEC10/COLEC11 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 10 isoforms produced by Alternative splicing.
Q9BWP8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsCL-K1-I
- Length271
- Mass (Da)28,665
- Last updated2001-06-01 v1
- ChecksumA14A248CE41DB340
Q9BWP8-2
- Name2
- SynonymsCL-K1-Ia
- Differences from canonical
- 43-66: Missing
Q9BWP8-3
- Name3
- SynonymsCL-K1-Ib
- Differences from canonical
- 67-90: Missing
Q9BWP8-4
- Name4
- SynonymsCL-K1-II
- Differences from canonical
- 1-43: MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLK → MWWVPPSPYGCLPCALP
Q9BWP8-5
- Name5
- SynonymsCL-K1-Ic
- Differences from canonical
- 43-90: Missing
Q9BWP8-6
- Name6
- SynonymsCL-K1-IIa
Q9BWP8-7
- Name7
- SynonymsCL-K1-IIb
Q9BWP8-8
- Name8
- SynonymsCL-K1-IIc
Q9BWP8-9
- Name9
- Differences from canonical
- 1-67: MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEK → MTPALCRSSSLASKGMRERRETKAPPDGLEESAPREKKQSQPVVTASDISKRKCTSSFVEMGSQ
Q9BWP8-10
- Name10
- Differences from canonical
- 1-1: M → MKKQRGVGVLPALRM
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045532 | 1 | in isoform 10 | |||
Sequence: M → MKKQRGVGVLPALRM | ||||||
Alternative sequence | VSP_030466 | 1-43 | in isoform 4 and isoform 7 | |||
Sequence: MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLK → MWWVPPSPYGCLPCALP | ||||||
Alternative sequence | VSP_030465 | 1-50 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_030464 | 1-67 | in isoform 9 | |||
Sequence: MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEK → MTPALCRSSSLASKGMRERRETKAPPDGLEESAPREKKQSQPVVTASDISKRKCTSSFVEMGSQ | ||||||
Alternative sequence | VSP_030463 | 1-74 | in isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_030468 | 43-66 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_030467 | 43-90 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_030469 | 51-67 | in isoform 6 | |||
Sequence: DKGAPGRPGRVGPTGEK → MWWVPPSPYGCLPCALP | ||||||
Alternative sequence | VSP_030470 | 67-90 | in isoform 3 and isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_030471 | 75-91 | in isoform 8 | |||
Sequence: QKGSVGRHGKIGPIGSK → MWWVPPSPYGCLPCALP | ||||||
Sequence conflict | 178 | in Ref. 7; CAI56781 | ||||
Sequence: S → T | ||||||
Sequence conflict | 231 | in Ref. 3; BAG64772 | ||||
Sequence: G → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB119525 EMBL· GenBank· DDBJ | BAF43301.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119650 EMBL· GenBank· DDBJ | BAF43302.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119651 EMBL· GenBank· DDBJ | BAF43303.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119652 EMBL· GenBank· DDBJ | BAF43304.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119684 EMBL· GenBank· DDBJ | BAF79604.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119685 EMBL· GenBank· DDBJ | BAF79605.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119686 EMBL· GenBank· DDBJ | BAF79606.1 EMBL· GenBank· DDBJ | mRNA | ||
AB119687 EMBL· GenBank· DDBJ | BAF79607.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358439 EMBL· GenBank· DDBJ | AAQ88805.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303824 EMBL· GenBank· DDBJ | BAG64772.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313840 EMBL· GenBank· DDBJ | BAG36572.1 EMBL· GenBank· DDBJ | mRNA | ||
AC010907 EMBL· GenBank· DDBJ | AAY24235.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX01053.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX01054.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX01055.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000078 EMBL· GenBank· DDBJ | AAH00078.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009951 EMBL· GenBank· DDBJ | AAH09951.1 EMBL· GenBank· DDBJ | mRNA | ||
CR936641 EMBL· GenBank· DDBJ | CAI56781.1 EMBL· GenBank· DDBJ | mRNA |